7XBL

Dimeric structure of human galectin-7 in complex with three glycerol

7XBL の概要

• エントリーDOI: 10.2210/pdb7xbl/pdb
• 分子名称: Galectin-7, GLYCEROL (3 entities in total)
• 機能のキーワード: promoting apoptosis binding glycerol, sugar binding protein
• 由来する生物種: Homo sapiens (human)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 30470.37

構造登録者

Si, Y.L. (登録日: 2022-03-21, 公開日: 2023-01-11, 最終更新日: 2023-11-29)

主引用文献

Liang, Y.,Wang, Y.,Zhu, X.,Cai, J.,Shi, A.,Huang, J.,Zhu, Q.,Si, Y.
Binding of Glycerol to Human Galectin-7 Expands Stability and Modulates Its Functions.
Int J Mol Sci, 23:-, 2022

PubMed Abstract: Glycerol is seen in biological systems as an intermediate in lipid metabolism. In recent years, glycerol has been reported to act as a chemical chaperone to correct the conformation of proteins. Here, we investigate the role of glycerol in galectin-7 (Gal-7). The thermal shift and CD assays showed that the thermal stability of Gal-7 increased with glycerol concentration but with little secondary structure changes induced by glycerol. In addition, glycerol can inhibit Gal-7-mediated erythrocyte agglutination. We also solved the crystal structures of human Gal-7 in complex with glycerol in two different conditions. Glycerol binds at the carbohydrate-recognition binding sites of Gal-7, which indicates glycerol as a small ligand for Gal-7. Surprisingly, glycerol can bind a new pocket near the N-terminus of Gal-7, which can greatly reduce the flexibility and improve the stability of this region. Moreover, overexpression of Gal-7 decreased the intracellular triglyceride levels and increased mRNA expression of aquaporin-3 (AQP-3) when HeLa cells were incubated with glycerol. These findings indicate that Gal-7 might regulate glycerol metabolism. Overall, our results on human Gal-7 raise the perspective to systematically explore this so far unrecognized phenomenon for Gal-7 in glycerol metabolism.

PubMed: 36293173
DOI: 10.3390/ijms232012318

実験手法

X-RAY DIFFRACTION (2 Å)